Protein S-Nitrosylation: Enzymatically Controlled, but Intrinsically Unstable, Post-translational Modification

Mol Cell. 2018 Feb 1;69(3):351-353. doi: 10.1016/j.molcel.2018.01.022.

Abstract

Reports by Seth et al. (2018) and Wolhuter et al. (2018) in this issue of Molecular Cell highlight the enzymatic synthesis, functionality, and propagation of S-nitrosylation-based signaling and address its low stability due to the elevated reactivity toward other cellular thiols.

Publication types

  • Research Support, Non-U.S. Gov't
  • Comment

MeSH terms

  • Nitric Oxide*
  • Protein Processing, Post-Translational
  • Protein S*
  • Proteolysis
  • Signal Transduction

Substances

  • Protein S
  • Nitric Oxide